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Conserved domains on  [gi|4646218|gb|AAD26884|]
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putative nucleotide-binding protein [Arabidopsis thaliana]

Protein Classification

large subunit GTPase 1 family protein( domain architecture ID 11439332)

large subunit GTPase 1 family protein similar to Mus musculus large subunit GTPase 1 homolog, which is required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit; probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm

EC:  3.6.1.-
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  11916378

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 157-362 3.71e-80

A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.


:

Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 247.15  E-value: 3.71e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  157 IWRQLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSAK 236
Cdd:cd01857   1 VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPSKENVLLLNKADLVTEEQRKAWARYFKKEGIVVLFFSAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  237 AATatlegkplkeqwrapdttqktdnpavkvygrddlldrlklealeivkmrksrgvsatsteshceqvVVGFVGYPNVG 316
Cdd:cd01857  81 NEA------------------------------------------------------------------TIGLVGYPNVG 94

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4646218  317 KSSTINALVGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPGLVFP 362
Cdd:cd01857  95 KSSLINALVGSKKVSVSSTPGKTKHFQTIFLEPGITLCDCPGLVFP 140
GTPase_YlqF super family cl37295
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 159-462 1.44e-29

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


The actual alignment was detected with superfamily member TIGR03596:

Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 117.61  E-value: 1.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218    159 RQLWRVLERSDLIVMVVDARDPLFYRCPDLEayaqEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSAKaa 238
Cdd:TIGR03596  13 REIKENLKLVDVVIEVLDARIPLSSRNPMID----EIRGNKPRLIVLNKADLADPAVTKQWLKYFEEKGIKALAVNAK-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218    239 tatlEGKPLKEqwrapdttqktdnpavkvygrddLLDRLKLEALEIVKMRKSRGVSATSTeshceQVVVgfVGYPNVGKS 318
Cdd:TIGR03596  87 ----KGAGVKK-----------------------IIKAAKKLLKEKNEKLKAKGLKNRPI-----RAMI--VGIPNVGKS 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218    319 STINALVGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPGLVFPSFSSSR--YEMVASG-----VLPIDRMTehLEAIKV 391
Cdd:TIGR03596 133 TLINRLAGKKVAKVGNRPGVTKGQQWIKLSDNLELLDTPGILWPKFEDQEvgLKLAATGaikdeALDLEDVA--LFLLEY 210

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4646218    392 VAELVPRhAIEDVYNIslpkpkSYEPQSrpplASELLRTYCLSRGYVASSGLPDETRAARQILKDYIEGKL 462
Cdd:TIGR03596 211 LLEHYPE-LLKERYKL------DELPED----PVELLEAIAKKRGCLLKGGELDLDRAAEILLNDFRKGKL 270
 
Name Accession Description Interval E-value
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 157-362 3.71e-80

A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 247.15  E-value: 3.71e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  157 IWRQLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSAK 236
Cdd:cd01857   1 VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPSKENVLLLNKADLVTEEQRKAWARYFKKEGIVVLFFSAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  237 AATatlegkplkeqwrapdttqktdnpavkvygrddlldrlklealeivkmrksrgvsatsteshceqvVVGFVGYPNVG 316
Cdd:cd01857  81 NEA------------------------------------------------------------------TIGLVGYPNVG 94

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4646218  317 KSSTINALVGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPGLVFP 362
Cdd:cd01857  95 KSSLINALVGSKKVSVSSTPGKTKHFQTIFLEPGITLCDCPGLVFP 140
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 159-462 1.44e-29

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 117.61  E-value: 1.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218    159 RQLWRVLERSDLIVMVVDARDPLFYRCPDLEayaqEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSAKaa 238
Cdd:TIGR03596  13 REIKENLKLVDVVIEVLDARIPLSSRNPMID----EIRGNKPRLIVLNKADLADPAVTKQWLKYFEEKGIKALAVNAK-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218    239 tatlEGKPLKEqwrapdttqktdnpavkvygrddLLDRLKLEALEIVKMRKSRGVSATSTeshceQVVVgfVGYPNVGKS 318
Cdd:TIGR03596  87 ----KGAGVKK-----------------------IIKAAKKLLKEKNEKLKAKGLKNRPI-----RAMI--VGIPNVGKS 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218    319 STINALVGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPGLVFPSFSSSR--YEMVASG-----VLPIDRMTehLEAIKV 391
Cdd:TIGR03596 133 TLINRLAGKKVAKVGNRPGVTKGQQWIKLSDNLELLDTPGILWPKFEDQEvgLKLAATGaikdeALDLEDVA--LFLLEY 210

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4646218    392 VAELVPRhAIEDVYNIslpkpkSYEPQSrpplASELLRTYCLSRGYVASSGLPDETRAARQILKDYIEGKL 462
Cdd:TIGR03596 211 LLEHYPE-LLKERYKL------DELPED----PVELLEAIAKKRGCLLKGGELDLDRAAEILLNDFRKGKL 270
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
159-462 2.61e-29

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 116.75  E-value: 2.61e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  159 RQLWRVLERSDLIVMVVDARDPLFYRCPDLEayaqEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSAKaa 238
Cdd:COG1161  15 RQIKEILKLVDLVIEVVDARIPLSSRNPMLD----ELVGNKPRLLVLNKADLADPSVTKQWLKYFEKQGVDALAISAK-- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  239 tatlEGKPLKEqwrapdttqktdnpavkvygrddLLDRLKLEALEIVKMRKSRgvsatsteshceQVVVgfVGYPNVGKS 318
Cdd:COG1161  89 ----KGKGIKE-----------------------LIEAIRELAPEKGIKRRPI------------RVMI--VGIPNVGKS 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  319 STINALVGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPGLVFPSFSSSR--YEMVASG-----VLPIDrmTEHLEAIKV 391
Cdd:COG1161 128 TLINRLAGKKVAKTGNKPGVTKGQQWIKLDDGLELLDTPGILWPKFEDPEvgYKLAATGaikdeVLDLE--EVALFLLGY 205

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4646218  392 VAELVPrHAIEDVYNIslpkpksyEPQSRPPLasELLRTYCLSRGYVASSGLPDETRAARQILKDYIEGKL 462
Cdd:COG1161 206 LARRYP-ELLKERYKL--------DELPRTKL--ELLEAIGRKRGCLLSGGEVDLEKAAEILLTDFRSGKL 265
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 307-360 7.71e-15

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 70.73  E-value: 7.71e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4646218    307 VGFVGYPNVGKSSTINALVGqKRTGVTSTPGKTKHFQTLIIS---EDLMLCDCPGLV 360
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTG-AKAIVSDYPGTTRDPNEGRLElkgKQIILVDTPGLI 57
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 307-358 2.76e-11

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 62.49  E-value: 2.76e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4646218    307 VGFVGYPNVGKSSTINALVGQKRTGVTS-TPGKTKHFQTLIISEDLMLCDCPG 358
Cdd:TIGR03598  21 IAFAGRSNVGKSSLINALTNRKKLARTSkTPGRTQLINFFEVNDGFRLVDLPG 73
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 307-358 3.44e-11

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 62.40  E-value: 3.44e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4646218  307 VGFVGYPNVGKSSTINALVGQK---RTGvtSTPGKTK---HFQtliISEDLMLCDCPG 358
Cdd:COG0218  26 IAFAGRSNVGKSSLINALTNRKklaRTS--KTPGKTQlinFFL---INDKFYLVDLPG 78
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 165-339 7.83e-07

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 51.59  E-value: 7.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218   165 LERSDLIVMVVDARDPLfyrCPDLEAYAQEI-DEHKKTMLLVNKADllPSYVREKWAEYFS--RNNILFVfwSAkaatat 241
Cdd:PRK00093  78 IEEADVILFVVDGRAGL---TPADEEIAKILrKSNKPVILVVNKVD--GPDEEADAYEFYSlgLGEPYPI--SA------ 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218   242 legkplkeqwrapdttqktdnpavkVYGR--DDLLDRLkLEALEivkmrksrgvSATSTESHCEQVVVGFVGYPNVGKSS 319
Cdd:PRK00093 145 -------------------------EHGRgiGDLLDAI-LEELP----------EEEEEDEEDEPIKIAIIGRPNVGKSS 188

                        170       180
                 ....*....|....*....|
gi 4646218   320 TINALVGQKRTGVTSTPGKT 339
Cdd:PRK00093 189 LINALLGEERVIVSDIAGTT 208
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 269-340 9.78e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 42.09  E-value: 9.78e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4646218   269 GRDDLLDrlklEALEivKMRKSRGVSATSTESHCEQVVVgfVGYPNVGKSSTINALVGQKRTGVTSTPGKTK 340
Cdd:PRK09518 423 GVGDLLD----EALD--SLKVAEKTSGFLTPSGLRRVAL--VGRPNVGKSSLLNQLTHEERAVVNDLAGTTR 486
 
Name Accession Description Interval E-value
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 157-362 3.71e-80

A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 247.15  E-value: 3.71e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  157 IWRQLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSAK 236
Cdd:cd01857   1 VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPSKENVLLLNKADLVTEEQRKAWARYFKKEGIVVLFFSAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  237 AATatlegkplkeqwrapdttqktdnpavkvygrddlldrlklealeivkmrksrgvsatsteshceqvVVGFVGYPNVG 316
Cdd:cd01857  81 NEA------------------------------------------------------------------TIGLVGYPNVG 94

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4646218  317 KSSTINALVGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPGLVFP 362
Cdd:cd01857  95 KSSLINALVGSKKVSVSSTPGKTKHFQTIFLEPGITLCDCPGLVFP 140
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 169-358 2.49e-30

A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein.


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 116.52  E-value: 2.49e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  169 DLIVMVVDARDPLFYRCPDLEAYAQEIDEHKKTMLLVNKADLLPSYVREKWAEYFsRNN---ILFvfwsaKAAT---ATL 242
Cdd:cd04178   1 DVILEVLDARDPLGCRCPQVERAVLVLGPNKKLVLVLNKIDLVPKENVEKWLKYL-RNEfptVAF-----KASTqqqKKN 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  243 EGKPLKEQWRAPDTTQKTdnpavKVYGRDDLLDRLKlealeivkmRKSRGVSATSTeshceqVVVGFVGYPNVGKSSTIN 322
Cdd:cd04178  75 LSRKSKKVKASDDLLSSS-----ACLGADALLKLLK---------NYARNKGIKTS------ITVGVVGYPNVGKSSVIN 134

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4646218  323 ALVGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPG 358
Cdd:cd04178 135 SLKRSRACNVGATPGVTKSMQEVHLDKHVKLLDSPG 170
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 157-358 2.63e-30

An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 115.88  E-value: 2.63e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  157 IWRQLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEIDehKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSAK 236
Cdd:cd01859   1 WKRLVRRIIKEADVVLEVVDARDPELTRSRKLERMALELG--KKLIIVLNKADLVPREVLEKWKEVFESEGLPVVYVSAR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  237 aatatlegkplkeqwrapdttqktdnpavKVYGRDDLLDRLKLEALEIvkmrksrgvsatsteshcEQVVVGFVGYPNVG 316
Cdd:cd01859  79 -----------------------------ERLGTRILRRTIKELAIDG------------------KPVIVGVVGYPKVG 111

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 4646218  317 KSSTINALVGQKRTGVTSTPGK---TKHFQTLIISEDLMLCDCPG 358
Cdd:cd01859 112 KSSIINALKGRHSASTSPIPGSpgyTKGIQLVRIDSKIYLIDTPG 156
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 160-358 3.71e-30

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with NKXD motif) are relocated to the N terminus.


Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 115.47  E-value: 3.71e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  160 QLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSakaat 239
Cdd:cd01858   1 ELYKVIDSSDVIIQVLDARDPMGTRCKHVEKYLRKEKPHKHLIFVLNKCDLVPTWVTKRWVKVLSKEYPTLAFHA----- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  240 atlegkplkeqwrapdttqKTDNPavkvYGRDDLLDRLKlealEIVKMRKSRgvsatsteshcEQVVVGFVGYPNVGKSS 319
Cdd:cd01858  76 -------------------SITNP----FGKGALINLLR----QFAKLHSDK-----------KQISVGFIGYPNVGKSS 117

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4646218  320 TINALVGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPG 358
Cdd:cd01858 118 VINTLRSKKVCKVAPIPGETKVWQYITLMKRIYLIDCPG 156
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 159-462 1.44e-29

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 117.61  E-value: 1.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218    159 RQLWRVLERSDLIVMVVDARDPLFYRCPDLEayaqEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSAKaa 238
Cdd:TIGR03596  13 REIKENLKLVDVVIEVLDARIPLSSRNPMID----EIRGNKPRLIVLNKADLADPAVTKQWLKYFEEKGIKALAVNAK-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218    239 tatlEGKPLKEqwrapdttqktdnpavkvygrddLLDRLKLEALEIVKMRKSRGVSATSTeshceQVVVgfVGYPNVGKS 318
Cdd:TIGR03596  87 ----KGAGVKK-----------------------IIKAAKKLLKEKNEKLKAKGLKNRPI-----RAMI--VGIPNVGKS 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218    319 STINALVGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPGLVFPSFSSSR--YEMVASG-----VLPIDRMTehLEAIKV 391
Cdd:TIGR03596 133 TLINRLAGKKVAKVGNRPGVTKGQQWIKLSDNLELLDTPGILWPKFEDQEvgLKLAATGaikdeALDLEDVA--LFLLEY 210

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4646218    392 VAELVPRhAIEDVYNIslpkpkSYEPQSrpplASELLRTYCLSRGYVASSGLPDETRAARQILKDYIEGKL 462
Cdd:TIGR03596 211 LLEHYPE-LLKERYKL------DELPED----PVELLEAIAKKRGCLLKGGELDLDRAAEILLNDFRKGKL 270
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
159-462 2.61e-29

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 116.75  E-value: 2.61e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  159 RQLWRVLERSDLIVMVVDARDPLFYRCPDLEayaqEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSAKaa 238
Cdd:COG1161  15 RQIKEILKLVDLVIEVVDARIPLSSRNPMLD----ELVGNKPRLLVLNKADLADPSVTKQWLKYFEKQGVDALAISAK-- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  239 tatlEGKPLKEqwrapdttqktdnpavkvygrddLLDRLKLEALEIVKMRKSRgvsatsteshceQVVVgfVGYPNVGKS 318
Cdd:COG1161  89 ----KGKGIKE-----------------------LIEAIRELAPEKGIKRRPI------------RVMI--VGIPNVGKS 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  319 STINALVGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPGLVFPSFSSSR--YEMVASG-----VLPIDrmTEHLEAIKV 391
Cdd:COG1161 128 TLINRLAGKKVAKTGNKPGVTKGQQWIKLDDGLELLDTPGILWPKFEDPEvgYKLAATGaikdeVLDLE--EVALFLLGY 205

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4646218  392 VAELVPrHAIEDVYNIslpkpksyEPQSRPPLasELLRTYCLSRGYVASSGLPDETRAARQILKDYIEGKL 462
Cdd:COG1161 206 LARRYP-ELLKERYKL--------DELPRTKL--ELLEAIGRKRGCLLSGGEVDLEKAAEILLTDFRSGKL 265
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 169-359 1.66e-28

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 110.55  E-value: 1.66e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  169 DLIVMVVDARDPLFYRCPDLEayaQEIDEH-KKTMLLVNKADLLPSYVREKWAEYFSRN-NILFVFWSAKaatatlEGKP 246
Cdd:cd01849   1 DVVVEVVDARDPLSSRNPDIE---VLINEKnKKLIMVLNKADLVPKEVLRKWVAELSELyGTKTFFISAT------NGQG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  247 LKEqwrapdttqktdnpavkvygrddlldrLKLEALEIVKMRKSRGvsatsteshceQVVVGFVGYPNVGKSSTINALVG 326
Cdd:cd01849  72 ILK---------------------------LKAEITKQKLKLKYKK-----------GIRVGVVGLPNVGKSSFINALLN 113

                       170       180       190
                ....*....|....*....|....*....|...
gi 4646218  327 QKRTGVTSTPGKTKHFQTLIISEDLMLCDCPGL 359
Cdd:cd01849 114 KFKLKVGSIPGTTKLQQDVKLDKEIYLYDTPGI 146
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 165-358 5.84e-24

Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 98.37  E-value: 5.84e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  165 LERSDLIVMVVDARDPLFYRCPDLEayaqEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFwsakaatatleg 244
Cdd:cd01856  17 LKLVDVVIEVRDARIPLSSRNPDLD----KILGNKPRLIVLNKADLADPAKTKKWLKYFKSQGEPVLF------------ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  245 kplkeqwrapdttqkTDnpAVKVYGRDDLLDRLKLEALEIVKMRKSRGVSATsteshceqVVVGFVGYPNVGKSSTINAL 324
Cdd:cd01856  81 ---------------VN--AKNGKGVKKLLKKAKKLLKENEKLKAKGLLPRP--------LRAMVVGIPNVGKSTLINRL 135

                       170       180       190
                ....*....|....*....|....*....|....
gi 4646218  325 VGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPG 358
Cdd:cd01856 136 RGKKVAKVGNKPGVTRGQQWIRIGPNIELLDTPG 169
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 307-360 7.71e-15

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 70.73  E-value: 7.71e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4646218    307 VGFVGYPNVGKSSTINALVGqKRTGVTSTPGKTKHFQTLIIS---EDLMLCDCPGLV 360
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTG-AKAIVSDYPGTTRDPNEGRLElkgKQIILVDTPGLI 57
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 307-358 5.14e-12

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 64.07  E-value: 5.14e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 4646218  307 VGFVGYPNVGKSSTINALVGQKRTGVTS-TPGKTKHFQTLIISEDLMLCDCPG 358
Cdd:cd01876   2 VAFAGRSNVGKSSLINALTNRKKLARTSkTPGRTQLINFFNVGDKFRLVDLPG 54
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 307-358 2.76e-11

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 62.49  E-value: 2.76e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4646218    307 VGFVGYPNVGKSSTINALVGQKRTGVTS-TPGKTKHFQTLIISEDLMLCDCPG 358
Cdd:TIGR03598  21 IAFAGRSNVGKSSLINALTNRKKLARTSkTPGRTQLINFFEVNDGFRLVDLPG 73
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 307-358 3.44e-11

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 62.40  E-value: 3.44e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4646218  307 VGFVGYPNVGKSSTINALVGQK---RTGvtSTPGKTK---HFQtliISEDLMLCDCPG 358
Cdd:COG0218  26 IAFAGRSNVGKSSLINALTNRKklaRTS--KTPGKTQlinFFL---INDKFYLVDLPG 78
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 147-359 1.12e-09

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 58.04  E-value: 1.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  147 VLTPFEKNLDIWRQLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEidehKKTMLLVNKADLLP---------SYVRE 217
Cdd:cd01855  13 LLDVEIPDEDFLEILSTLLNDNALVVHVVDIFDFPGSLIPGLAELIGA----KPVILVGNKIDLLPkdvkpnrlkQWVKK 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  218 KWAEYFSRN-NILFVfwSAKaatatlegkplkeqwrapdttqktdnpavKVYGRDDLLDRLKlealeivKMRKSRGVsat 296
Cdd:cd01855  89 RLKIGGLKIkDVILV--SAK-----------------------------KGWGVEELIEEIK-------KLAKYRGD--- 127

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4646218  297 steshceqvvVGFVGYPNVGKSSTINALVGQK-----------RTGVTSTPGKTKHFQTLIISEDLMLCDCPGL 359
Cdd:cd01855 128 ----------VYVVGATNVGKSTLINALLKSNggkvqaqalvqRLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
140-339 3.17e-09

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 59.27  E-value: 3.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  140 LEENEKlvlTPFEKnlDIWRQLWRVLERSDLIVMVVDARDPLfyrCPDLEAYAQEIDEHKK-TMLLVNKADllpSYVREK 218
Cdd:COG1160  60 IEPDDD---DGLEA--EIREQAELAIEEADVILFVVDGRAGL---TPLDEEIAKLLRRSGKpVILVVNKVD---GPKREA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  219 WAEYFSR---NNILFVfwSAkaatatLEGKplkeqwrapdttqktdnpavkvyGRDDLLDRLkLEALEivkmrksrgvsA 295
Cdd:COG1160 129 DAAEFYSlglGEPIPI--SA------EHGR-----------------------GVGDLLDAV-LELLP-----------E 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 4646218  296 TSTESHCEQVV-VGFVGYPNVGKSSTINALVGQKRTGVTSTPGKT 339
Cdd:COG1160 166 EEEEEEEDDPIkIAIVGRPNVGKSSLINALLGEERVIVSDIAGTT 210
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 308-359 2.32e-08

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 53.40  E-value: 2.32e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4646218  308 GFVGYPNVGKSSTINALVGQKRTGVTSTPGKTKHFQ----TLIISEDLMLCDCPGL 359
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVrkewELLPLGPVVLIDTPGL 56
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 308-360 3.14e-08

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 53.23  E-value: 3.14e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4646218  308 GFVGYPNVGKSSTINALVGQKRTGVTSTPGKT-----KHFQTLIISEDLMLCDCPGLV 360
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTrdpdvYVKELDKGKVKLVLVDTPGLD 58
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 165-339 7.83e-07

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 51.59  E-value: 7.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218   165 LERSDLIVMVVDARDPLfyrCPDLEAYAQEI-DEHKKTMLLVNKADllPSYVREKWAEYFS--RNNILFVfwSAkaatat 241
Cdd:PRK00093  78 IEEADVILFVVDGRAGL---TPADEEIAKILrKSNKPVILVVNKVD--GPDEEADAYEFYSlgLGEPYPI--SA------ 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218   242 legkplkeqwrapdttqktdnpavkVYGR--DDLLDRLkLEALEivkmrksrgvSATSTESHCEQVVVGFVGYPNVGKSS 319
Cdd:PRK00093 145 -------------------------EHGRgiGDLLDAI-LEELP----------EEEEEDEEDEPIKIAIIGRPNVGKSS 188

                        170       180
                 ....*....|....*....|
gi 4646218   320 TINALVGQKRTGVTSTPGKT 339
Cdd:PRK00093 189 LINALLGEERVIVSDIAGTT 208
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 307-339 2.23e-06

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 47.81  E-value: 2.23e-06
                        10        20        30
                ....*....|....*....|....*....|...
gi 4646218  307 VGFVGYPNVGKSSTINALVGQKRTGVTSTPGKT 339
Cdd:cd01895   5 IAIIGRPNVGKSSLLNALLGEERVIVSDIAGTT 37
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 307-362 2.88e-06

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 47.46  E-value: 2.88e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4646218  307 VGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTKHFQTLIISED---LMLCDCPGLVFP 362
Cdd:cd04163   6 VAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDdaqIIFVDTPGIHKP 64
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 155-232 2.36e-05

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 44.75  E-value: 2.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  155 LDIWRQLWRVLERSDLIVMVVDARDP-LFYRCPDLeaYAQEIDEHKKTMLLV-NKADLLPSYVREKW--AEYFSRNNILF 230
Cdd:cd00882  63 LGREELARLLLRGADLILLVVDSTDReSEEDAKLL--ILRRLRKEGIPIILVgNKIDLLEEREVEELlrLEELAKILGVP 140


                ..
gi 4646218  231 VF 232
Cdd:cd00882 141 VF 142
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 310-339 7.45e-05

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 43.25  E-value: 7.45e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 4646218  310 VGYPNVGKSSTINALVGQKRTGVTSTPGKT 339
Cdd:cd04164   9 AGKPNVGKSSLLNALAGRDRAIVSDIAGTT 38
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
307-359 8.95e-05

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 44.59  E-value: 8.95e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4646218  307 VGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTKHFQTLIISED---LMLCDCPGL 359
Cdd:COG1159   6 VAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREdaqIVFVDTPGI 61
era PRK00089
GTPase Era; Reviewed
 307-341 1.62e-04

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 43.88  E-value: 1.62e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 4646218   307 VGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTKH 341
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRH 42
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
276-360 1.63e-04

Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 44.02  E-value: 1.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  276 RLKLEaLEIVKMRKSRGVSATSTESHCE-QVVVgfVGYPNVGKSSTINALvgqkrTGVTSTPGkTKHFQTLIISEDLM-- 352
Cdd:COG1163  37 ELKEE-LEKRKKKSGGGGEGFAVKKSGDaTVVL--VGFPSVGKSTLLNKL-----TNAKSEVG-AYEFTTLDVVPGMLey 107

                        90
                ....*....|....
gi 4646218  353 ------LCDCPGLV 360
Cdd:COG1163 108 kgakiqILDVPGLI 121
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 162-236 1.78e-04

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 43.90  E-value: 1.78e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4646218  162 WRVLERSDLIVMVVDARDPLFyrcPDLEAYAQEIdEHKKTMLLVNKADLLPsyvrEKWAEYFSRNNILFVFWSAK 236
Cdd:COG0486 287 REAIEEADLVLLLLDASEPLT---EEDEEILEKL-KDKPVIVVLNKIDLPS----EADGELKSLPGEPVIAISAK 353
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 305-380 1.91e-04

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 41.97  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218    305 VVVGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTKHFQTLIISED-----LMLCDCPGLV-FPSFSSSRYEMVASGVLP 378
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDgktykFNLLDTAGQEdYDAIRRLYYPQVERSLRV 81


                  ..
gi 4646218    379 ID 380
Cdd:TIGR00231  82 FD 83
YeeP COG3596
Predicted GTPase [General function prediction only];
301-359 2.46e-04

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 43.22  E-value: 2.46e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4646218  301 HCEQVVVGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTKHFQTLIISED----LMLCDCPGL 359
Cdd:COG3596  36 ELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLESDglpgLVLLDTPGL 98
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
152-236 4.86e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 41.12  E-value: 4.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  152 EKNLDIW------------RQLWRVLERSDLIVMVVDARDPLFYRC-PDLEAYAQEIDEHKKTMLLVNKADLLPSYVREK 218
Cdd:COG1100  52 DVDLVIWdtpgqdefretrQFYARQLTGASLYLFVVDGTREETLQSlYELLESLRRLGKKSPIILVLNKIDLYDEEEIED 131

                        90       100
                ....*....|....*....|..
gi 4646218  219 W---AEYFSRNNILFVFW-SAK 236
Cdd:COG1100 132 EerlKEALSEDNIVEVVAtSAK 153
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 307-371 4.93e-04

GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]


Pssm-ID: 129528 [Multi-domain]  Cd Length: 270  Bit Score: 41.99  E-value: 4.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4646218    307 VGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTKHFQTLIISED---LMLCDCPGLVFPSFSSSRYEM 371
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGasqIIFIDTPGFHEKKHSLNRLMM 70
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 162-218 5.40e-04

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 40.69  E-value: 5.40e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4646218  162 WRVLERSDLIVMVVDARDPLFyrcpDLEAYAQEIDEHKKTMLLV-NKADLLPSYVREK 218
Cdd:cd00880  71 RQVADRADLVLLVVDSDLTPV----EEEAKLGLLRERGKPVLLVlNKIDLVPESEEEE 124
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 310-339 5.81e-04

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 42.08  E-value: 5.81e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 4646218    310 VGYPNVGKSSTINALVGQKRTGVTSTPGKT 339
Cdd:pfam12631 100 VGKPNVGKSSLLNALLGEERAIVTDIPGTT 129
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 269-340 9.78e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 42.09  E-value: 9.78e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4646218   269 GRDDLLDrlklEALEivKMRKSRGVSATSTESHCEQVVVgfVGYPNVGKSSTINALVGQKRTGVTSTPGKTK 340
Cdd:PRK09518 423 GVGDLLD----EALD--SLKVAEKTSGFLTPSGLRRVAL--VGRPNVGKSSLLNQLTHEERAVVNDLAGTTR 486
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 168-236 9.86e-04

HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 40.52  E-value: 9.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4646218  168 SDLIVMVVDARDplfyrcPDLEAYAQ-------EIDEHKKTMLLV-NKADLLPSYVREKWAEYfSRNNILFVfwSAK 236
Cdd:cd01878 121 ADLLLHVVDASD------PDREEQIEtveevlkELGADDIPIILVlNKIDLLDDEELEERLRA-GRPDAVFI--SAK 188
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 162-236 9.98e-04

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 39.79  E-value: 9.98e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4646218  162 WRVLERSDLIVMVVDARDPLfyrcPDLEAYAQEIDEHKKTMLLVNKADLLPSYVREKwaeYFSRNNILFVfwSAK 236
Cdd:cd04164  77 REAIEEADLVLLVVDASEGL----DEEDLEILELPAKKPVIVVLNKSDLLSDAEGIS---ELNGKPIIAI--SAK 142
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 163-236 1.10e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 41.57  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218   163 RVLERSDLIVMVVDARDPlfyrcpdLEAY----AQEIDEHKK-TMLLVNKADLLPSYVREKWAEYFSRN-------NILF 230
Cdd:PRK00093 251 KAIERADVVLLVIDATEG-------ITEQdlriAGLALEAGRaLVIVVNKWDLVDEKTMEEFKKELRRRlpfldyaPIVF 323


                 ....*.
gi 4646218   231 VfwSAK 236
Cdd:PRK00093 324 I--SAL 327
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 162-236 1.15e-03

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 41.31  E-value: 1.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4646218    162 WRVLERSDLIVMVVDARDPLFyrcPDLEAYAQEIDEHKKTMLLVNKADLLPSYVREKWAEyfsrnNILFVFWSAK 236
Cdd:pfam12631 168 REAIEEADLVLLVLDASRPLD---EEDLEILELLKDKKPIIVVLNKSDLLGEIDELEELK-----GKPVLAISAK 234
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 310-339 1.51e-03

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 41.20  E-value: 1.51e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 4646218  310 VGYPNVGKSSTINALVGQKRTGVTSTPGKT 339
Cdd:COG0486 219 VGRPNVGKSSLLNALLGEERAIVTDIAGTT 248
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
310-339 1.65e-03

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 40.86  E-value: 1.65e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 4646218   310 VGYPNVGKSSTINALVGQKRTGVTSTPGKT 339
Cdd:PRK05291 221 AGRPNVGKSSLLNALLGEERAIVTDIAGTT 250
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 162-236 1.93e-03

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 39.37  E-value: 1.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  162 WRVLERSDLIVMVVDARDPLfyrCPDLEAYAQEIDEHKKTMLLV-NKADLLPSyvREKWAEYFSRNNILFVFW-----SA 235
Cdd:cd04163  77 WSALKDVDLVLFVVDASEWI---GEGDEFILELLKKSKTPVILVlNKIDLVKD--KEDLLPLLEKLKELHPFAeifpiSA 151


                .
gi 4646218  236 K 236
Cdd:cd04163 152 L 152
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
162-236 2.40e-03

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 40.48  E-value: 2.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4646218   162 WRVLERSDLIVMVVDARDPLFyrCPDLEAYAQEidEHKKTMLLVNKADLLPsyvrEKWAEYFSRNNILFVfwSAK 236
Cdd:PRK05291 289 REAIEEADLVLLVLDASEPLT--EEDDEILEEL--KDKPVIVVLNKADLTG----EIDLEEENGKPVIRI--SAK 353
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 307-339 2.57e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 40.34  E-value: 2.57e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 4646218   307 VGFVGYPNVGKSSTINALVGQKRTGVTSTPGKT 339
Cdd:PRK03003 214 VALVGKPNVGKSSLLNKLAGEERSVVDDVAGTT 246
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 163-236 3.34e-03

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 38.57  E-value: 3.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  163 RVLERSDLIVMVVDARDPLfyrcPDLEAY-AQEIDEHKK-TMLLVNKADLLP--SYVREKWAEYFsRNNILFVFW----- 233
Cdd:cd01895  80 KAIERADVVLLVLDASEGI----TEQDLRiAGLILEEGKaLIIVVNKWDLVEkdEKTMKEFEKEL-RRKLPFLDYapivf 154


                ....
gi 4646218  234 -SAK 236
Cdd:cd01895 155 iSAL 158
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 307-324 3.45e-03

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 38.56  E-value: 3.45e-03
                        10
                ....*....|....*...
gi 4646218  307 VGFVGYPNVGKSSTINAL 324
Cdd:cd01898   3 VGLVGLPNAGKSTLLSAI 20
TIGR00157 TIGR00157
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and ...
 309-375 4.22e-03

ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and are now designated RsgA (ribosome small subunit-dependent GTPase A). The strongest motif in the alignment of these proteins is GXSGVGKS[ST], a classic P-loop for nucleotide binding. This protein has been shown to cleave GTP and remain bound to GDP. A role as a regulator of translation has been suggested. The Aquifex aeolicus ortholog is split into consecutive open reading frames. Consequently, this model was build in fragment mode (-f option). [Protein synthesis, Translation factors]


Pssm-ID: 272934 [Multi-domain]  Cd Length: 245  Bit Score: 38.93  E-value: 4.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4646218    309 FVGYPNVGKSSTINAL---VGQKRTGVTSTPGKTKHFQTLIISEDL---MLCDCPGLVFPSFSSSRYEMVASG 375
Cdd:TIGR00157 125 FAGQSGVGKSSLINALdpsVKQQVNDISSKLGLGKHTTTHVELFHFhggLIADTPGFNEFGLWHLEPEQLTQG 197
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 306-340 5.19e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 39.57  E-value: 5.19e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 4646218   306 VVGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTK 340
Cdd:PRK03003  40 VVAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTR 74
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 307-360 6.30e-03

Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding.


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 38.30  E-value: 6.30e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4646218  307 VGFVGYPNVGKSSTINALVGQKR-------TGVTSTPGKTKHFQTLIisedlMLCDCPGLV 360
Cdd:cd01896   3 VALVGFPSVGKSTLLSKLTNTKSevaayefTTLTCVPGVMEYKGAKI-----QLLDLPGII 58
obgE PRK12297
GTPase CgtA; Reviewed
 307-324 6.32e-03

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 38.93  E-value: 6.32e-03
                         10
                 ....*....|....*...
gi 4646218   307 VGFVGYPNVGKSSTINAL 324
Cdd:PRK12297 161 VGLVGFPNVGKSTLLSVV 178
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 306-340 7.31e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 39.01  E-value: 7.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 4646218   306 VVGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTK 340
Cdd:PRK09518 277 VVAIVGRPNVGKSTLVNRILGRREAVVEDTPGVTR 311
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 148-224 7.70e-03

EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 37.41  E-value: 7.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  148 LTPFEKNLD--IWRQLWRVLERSDLIVMVVDARDPLfyrcpdleayaQEIDEH---------KKTMLLVNKADLLPSYVR 216
Cdd:cd01894  55 IEPDDEGISkeIREQAEIAIEEADVILFVVDGREGL-----------TPADEEiakylrkskKPVILVVNKIDNIKEEEE 123


                ....*...
gi 4646218  217 EkwAEYFS 224
Cdd:cd01894 124 A--AEFYS 129
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 307-324 8.62e-03

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 38.77  E-value: 8.62e-03
                         10
                 ....*....|....*...
gi 4646218   307 VGFVGYPNVGKSSTINAL 324
Cdd:PTZ00258  24 MGIVGLPNVGKSTTFNAL 41
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 305-339 9.43e-03

Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 37.04  E-value: 9.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 4646218    305 VVVGFVGYPNVGKSSTINALVGqKRTGVTSTPGKT 339
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTG-ANQHVGNWPGVT 34
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
163-236 9.66e-03

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 38.47  E-value: 9.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4646218  163 RVLERSDLIVMVVDARDPlfyrcpdLEAY----AQEIDEHKK-TMLLVNKADLLP--SYVREKWAEYFSRN-------NI 228
Cdd:COG1160 253 RAIERADVVLLVIDATEG-------ITEQdlkiAGLALEAGKaLVIVVNKWDLVEkdRKTREELEKEIRRRlpfldyaPI 325


                ....*...
gi 4646218  229 LFVfwSAK 236
Cdd:COG1160 326 VFI--SAL 331
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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